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Q13451 (FKBP5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase FKBP5

Short name=PPIase FKBP5
EC=5.2.1.8
Alternative name(s):
51 kDa FK506-binding protein
Short name=51 kDa FKBP
Short name=FKBP-51
54 kDa progesterone receptor-associated immunophilin
Androgen-regulated protein 6
FF1 antigen
FK506-binding protein 5
Short name=FKBP-5
FKBP54
Short name=p54
HSP90-binding immunophilin
Rotamase
Gene names
Name:FKBP5
Synonyms:AIG6, FKBP51
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length457 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Immunophilin protein with PPIase and co-chaperone activities. Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). Plays a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors maintaining the complex into the cytoplasm when unliganded.

Catalytic activity

Peptidylproline (omega=180) = peptidylproline (omega=0).

Enzyme regulation

Inhibited by FK506 but not cyclosporin.

Subunit structure

Part of a heteromultimeric cytoplasmic complex with HSP90AA1, HSPA1A/HSPA1B and steroid receptors. Upon ligand binding dissociates from the complex and FKBP4 takes its place. Interacts with functionally mature heterooligomeric progesterone receptor complexes along with HSP90 and TEBP.

Subcellular location

Cytoplasm. Nucleus.

Tissue specificity

Widely expressed, enriched in testis compared to other tissues.

Induction

By androgen.

Sequence similarities

Contains 2 PPIase FKBP-type domains.

Contains 3 TPR repeats.

Sequence caution

The sequence BAD93130.1 differs from that shown. Reason: Frameshift at position 29.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13451-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q13451-2)

The sequence of this isoform differs from the canonical sequence as follows:
     223-268: YGFGEAGKPK...MDTKEKLEQA → PKNPGRWIPK...SISKNLFKCW
     269-457: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 457457Peptidyl-prolyl cis-trans isomerase FKBP5
PRO_0000075324

Regions

Domain42 – 13089PPIase FKBP-type 1
Domain157 – 24387PPIase FKBP-type 2
Repeat268 – 30134TPR 1
Repeat317 – 35034TPR 2
Repeat351 – 38434TPR 3

Amino acid modifications

Modified residue11N-acetylmethionine Ref.12
Modified residue4451Phosphoserine Ref.10

Natural variations

Alternative sequence223 – 26846YGFGE…KLEQA → PKNPGRWIPKKNWSRLPLSK RREPYTSRCVSPYAILSISK NLFKCW in isoform 2.
VSP_044820
Alternative sequence269 – 457189Missing in isoform 2.
VSP_044821

Secondary structure

................................................................ 457
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: 18A86608C6891A73

FASTA45751,212
        10         20         30         40         50         60 
MTTDEGAKNN EESPTATVAE QGEDITSKKD RGVLKIVKRV GNGEETPMIG DKVYVHYKGK 

        70         80         90        100        110        120 
LSNGKKFDSS HDRNEPFVFS LGKGQVIKAW DIGVATMKKG EICHLLCKPE YAYGSAGSLP 

       130        140        150        160        170        180 
KIPSNATLFF EIELLDFKGE DLFEDGGIIR RTKRKGEGYS NPNEGATVEI HLEGRCGGRM 

       190        200        210        220        230        240 
FDCRDVAFTV GEGEDHDIPI GIDKALEKMQ REEQCILYLG PRYGFGEAGK PKFGIEPNAE 

       250        260        270        280        290        300 
LIYEVTLKSF EKAKESWEMD TKEKLEQAAI VKEKGTVYFK GGKYMQAVIQ YGKIVSWLEM 

       310        320        330        340        350        360 
EYGLSEKESK ASESFLLAAF LNLAMCYLKL REYTKAVECC DKALGLDSAN EKGLYRRGEA 

       370        380        390        400        410        420 
QLLMNEFESA KGDFEKVLEV NPQNKAARLQ ISMCQKKAKE HNERDRRIYA NMFKKFAEQD 

       430        440        450 
AKEEANKAMG KKTSEGVTNE KGTDSQAMEE EKPEGHV 

« Hide

Isoform 2 [UniParc].

Checksum: 2B172A6E03570AAD
Show »

FASTA26830,032

References

« Hide 'large scale' references
[1]"Tissue distribution and abundance of human FKBP51, an FK506-binding protein that can mediate calcineurin inhibition."
Baughman G., Wiederrecht G.J., Chang F., Martin M.M., Bourgeois S.
Biochem. Biophys. Res. Commun. 232:437-443(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Thymus.
[2]"Identification of AIG6 as an androgen response gene in human prostate cancer cell line LNCaP."
Zhang J.S., Smith D.I.
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[4]"Homo sapiens protein coding cDNA."
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Aortic endothelium.
[5]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Testis.
[8]"Molecular cloning of human FKBP51 and comparisons of immunophilin interactions with Hsp90 and progesterone receptor."
Nair S.C., Rimerman R.A., Toran E.J., Chen S., Prapapanich V., Butts R.N., Smith D.F.
Mol. Cell. Biol. 17:594-603(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-457 (ISOFORM 1).
[9]"FKBP54, a novel FK506-binding protein in avian progesterone receptor complexes and HeLa extracts."
Smith D.F., Albers M.W., Schreiber S.L., Leach K.L., Deibel M.R. Jr.
J. Biol. Chem. 268:24270-24273(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[10]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Structure of the large FK506-binding protein FKBP51, an Hsp90-binding protein and a component of steroid receptor complexes."
Sinars C.R., Cheung-Flynn J., Rimerman R.A., Scammell J.G., Smith D.F., Clardy J.
Proc. Natl. Acad. Sci. U.S.A. 100:868-873(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U71321 mRNA. Translation: AAC51189.1.
AF194172 mRNA. Translation: AAL54872.1.
AK312422 mRNA. Translation: BAG35332.1.
AB209893 mRNA. Translation: BAD93130.1. Frameshift.
AL033519 Genomic DNA. Translation: CAI20256.1.
AL157823 Genomic DNA. No translation available.
AL590400 Genomic DNA. No translation available.
CH471081 Genomic DNA. Translation: EAX03842.1.
BC042605 mRNA. Translation: AAH42605.1.
U42031 mRNA. Translation: AAA86245.1.
PIRJC5422.
RefSeqNP_001139247.1. NM_001145775.2.
NP_001139248.1. NM_001145776.1.
NP_001139249.1. NM_001145777.1.
NP_004108.1. NM_004117.3.
UniGeneHs.407190.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KT0X-ray2.70A1-457[»]
3O5DX-ray4.00A/B1-260[»]
3O5EX-ray1.60A1-140[»]
3O5FX-ray1.65A1-140[»]
3O5GX-ray2.00A16-140[»]
3O5IX-ray1.80A/B16-140[»]
3O5JX-ray1.70A16-140[»]
3O5KX-ray2.70A/B/C/D16-140[»]
3O5LX-ray1.30A16-140[»]
3O5MX-ray1.60A/B16-140[»]
3O5OX-ray1.15A16-140[»]
3O5PX-ray1.00A16-140[»]
3O5QX-ray0.96A16-140[»]
3O5RX-ray1.10A16-140[»]
4DRHX-ray2.30A/D1-140[»]
4DRIX-ray1.45A1-140[»]
4DRKX-ray1.50A/B16-140[»]
4DRMX-ray1.48A16-140[»]
4DRNX-ray1.07A16-140[»]
4DROX-ray1.10A16-140[»]
4DRPX-ray1.80A16-140[»]
4DRQX-ray1.00A16-140[»]
4JFIX-ray1.05A16-139[»]
4JFJX-ray1.08A16-140[»]
4JFKX-ray1.15A16-140[»]
4JFLX-ray1.20A16-140[»]
4JFMX-ray1.02A16-140[»]
ProteinModelPortalQ13451.
SMRQ13451. Positions 13-412.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108579. 35 interactions.
DIPDIP-27597N.
IntActQ13451. 18 interactions.
MINTMINT-1142816.
STRING9606.ENSP00000338160.

Chemistry

ChEMBLCHEMBL2052031.

PTM databases

PhosphoSiteQ13451.

Polymorphism databases

DMDM2851536.

Proteomic databases

PaxDbQ13451.
PRIDEQ13451.

Protocols and materials databases

DNASU2289.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000357266; ENSP00000349811; ENSG00000096060. [Q13451-1]
ENST00000536438; ENSP00000444810; ENSG00000096060. [Q13451-1]
ENST00000539068; ENSP00000441205; ENSG00000096060. [Q13451-1]
ENST00000542713; ENSP00000442340; ENSG00000096060. [Q13451-2]
GeneID2289.
KEGGhsa:2289.
UCSCuc003okx.2. human. [Q13451-1]

Organism-specific databases

CTD2289.
GeneCardsGC06M035541.
HGNCHGNC:3721. FKBP5.
HPACAB009315.
HPA031092.
HPA031093.
HPA031095.
MIM602623. gene.
neXtProtNX_Q13451.
PharmGKBPA28162.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0545.
HOGENOMHOG000256916.
HOVERGENHBG051624.
InParanoidQ13451.
KOK09571.
OMAHLEGCCG.
OrthoDBEOG725DHH.
PhylomeDBQ13451.
TreeFamTF105292.

Gene expression databases

ArrayExpressQ13451.
BgeeQ13451.
CleanExHS_FKBP5.
GenevestigatorQ13451.

Family and domain databases

Gene3D1.10.150.160. 1 hit.
1.25.40.10. 1 hit.
InterProIPR023114. Elongated_TPR_rpt_dom.
IPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERPTHR10516. PTHR10516. 1 hit.
PfamPF00254. FKBP_C. 2 hits.
PF00515. TPR_1. 2 hits.
[Graphical view]
PROSITEPS50059. FKBP_PPIASE. 2 hits.
PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFKBP5. human.
EvolutionaryTraceQ13451.
GeneWikiFKBP5.
GenomeRNAi2289.
NextBio9303.
PROQ13451.
SOURCESearch...

Entry information

Entry nameFKBP5_HUMAN
AccessionPrimary (citable) accession number: Q13451
Secondary accession number(s): F5H7R1, Q59EB8, Q5TGM6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 15, 1998
Last modified: April 16, 2014
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM